Crystallization (Comment) | Organism |
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hanging drop vapor diffusion method. X-ray crystal structure of the bifunctional enzyme in complex with UDP-GlcNAc and CoA, determined to 2.1 A resolution and reveals a two-domain architecture that is responsible for the two reactions of EC 2.3.1.157 and EC 2.7.7.23. The C-terminal domain is responsible for the CoA-dependent acetylation of Glc-1-phosphate to GlcNAc-1-phosphate and displays the longest left-handed parallel alpha-helix observed to date. The acetyltransferase active site defined by the binding site for CoA makes use of residues from all three subunits and is positioned beneath an open cavity large enough to accommodate the Glc-1-PO4 acetyl acceptor. The N-terminal domain catalyzes uridyl transfer from UTP to GlcNAc-1-phosphate to form the final products UDP-GlcNAc and pyrophosphate | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
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D-glucosamine 1-phosphate + acetyl-CoA | Escherichia coli | the bifunctional enzyme also possesses the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase and performs the last two steps in the synthesis of UDP-N-acetylglucosamine | N-acetyl-D-glucosamine 1-phosphate + CoA | - |
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Organism | UniProt | Comment | Textmining |
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Escherichia coli | P0ACC7 | - |
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Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
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D-glucosamine 1-phosphate + acetyl-CoA | the bifunctional enzyme also possesses the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase and performs the last two steps in the synthesis of UDP-N-acetylglucosamine | Escherichia coli | N-acetyl-D-glucosamine 1-phosphate + CoA | - |
? | |
D-glucosamine 1-phosphate + acetyl-CoA | the bifunctional enzyme also possesses the activity of EC 2.7.7.23. The C-terminal domain is responsible for the CoA-dependent acetylation of Glc-1-phosphate to GlcNAc-1-phosphate. The N-terminal domain catalyzes uridyl transfer from UTP to GlcNAc-1-phosphate to form the final products UDP-GlcNAc and pyrophosphate | Escherichia coli | N-acetyl-D-glucosamine 1-phosphate + CoA | - |
? |
Synonyms | Comment | Organism |
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N-acetylglucosamine-1-phosphate uridyltransferase | bifunctional enzyme also possesses the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase | Escherichia coli |